› 2lq4

Solution NMR

Structural Characterization of an LPA1 Second Extracellular Loop Mimetic with a Self-Assembling Coiled-Coil Folding Constraint

Released:
DOI: 10.2210/pdb2lq4/pdb
PDB entry 2lq4 coloured by chain, ensemble of 36 models, front view.
PDB entry 2lq4 coloured by chain, ensemble of 36 models, side view.
PDB entry 2lq4 coloured by chain, ensemble of 36 models, top view.
Source organism: synthetic construct
Primary publication:
Structural Characterization of an LPA1 Second Extracellular Loop Mimetic with a Self-Assembling Coiled-Coil Folding Constraint.
Young JK, Clayton BT, Kikonyogo A, Pham TC, Parrill AL
OpenAccess logo Int J Mol Sci 14 2788-807 (2013)
PMID: 23434648

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162915 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysophosphatidic acid receptor 1 Chain: p
Molecule details ›
Chain: p
Length: 80 amino acids
Theoretical weight: 9.34 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 80%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

2 review citations

LPA receptor signaling: pharmacology, physiology, and pathophysiology.
Yung et al. (2014)
1 more

2 mentions without citation

Lys39-Lysophosphatidate Carbonyl Oxygen Interaction Locks LPA1 N-terminal Cap to the Orthosteric Site and partners Arg124 During Receptor Activation.
Omotuyi et al. (2015)
1 more